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Conserved domains on  [gi|300797828|ref|NP_001178784|]
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cysteine-rich protein 2-binding protein [Rattus norvegicus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11688059)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 683-758 1.43e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 683 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 758
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 601-763 4.09e-03

N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase which catalyze the transfer of an acetyl group to a substrate. The mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and then CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK09831:

Pssm-ID: 473072  Cd Length: 147  Bit Score: 38.40  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 601 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 678
Cdd:PRK09831   4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 679 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 750
Cdd:PRK09831  56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                        170
                 ....*....|....
gi 300797828 751 -EEYVLDFYDKYYP 763
Cdd:PRK09831 132 rGEWFINFYMRYKP 145
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 683-758 1.43e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 683 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 758
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 669-748 8.90e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 62.54  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828  669 PDFSVVVLYKKVIVAF-GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLY 743
Cdd:pfam00583  32 SEGFFVAEEDGELVGFaSLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGcerIFLEVAADNlAAIALY 111


                  ....*
gi 300797828  744 QKFGF 748
Cdd:pfam00583 112 EKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 672-724 1.36e-05

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 43.42  E-value: 1.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300797828 672 SVVVLYKKVIVAFGFMVP-DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTC 724
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
PRK09831 PRK09831
GNAT family N-acetyltransferase;
601-763 4.09e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 38.40  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 601 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 678
Cdd:PRK09831   4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 679 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 750
Cdd:PRK09831  56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                        170
                 ....*....|....
gi 300797828 751 -EEYVLDFYDKYYP 763
Cdd:PRK09831 132 rGEWFINFYMRYKP 145
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 685-763 6.81e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 685 GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASN-PAMLLYQKFGFKTeeyvLDFYDK 760
Cdd:PRK09491  53 AFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVAtlwLEVRASNaAAIALYESLGFNE----VTIRRN 128


                 ...
gi 300797828 761 YYP 763
Cdd:PRK09491 129 YYP 131
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 683-758 1.43e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 683 AFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLYQKFGFKTEEYVLDFY 758
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGarrLRLEVREDNeAAIALYEKLGFEEVGERPNYY 80
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 669-748 8.90e-12

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 62.54  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828  669 PDFSVVVLYKKVIVAF-GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKD---VTLHVSASN-PAMLLY 743
Cdd:pfam00583  32 SEGFFVAEEDGELVGFaSLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGcerIFLEVAADNlAAIALY 111


                  ....*
gi 300797828  744 QKFGF 748
Cdd:pfam00583 112 EKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 673-778 1.91e-09

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 56.54  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 673 VVVLYKKVIVAFGFMVPDVKyNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDV-TLHVSASNPAMLLYQKFGFKte 751
Cdd:COG1246   31 WVAEEDGEIVGCAALHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLkRLFLLTTSAAIHFYEKLGFE-- 107

                         90       100
                 ....*....|....*....|....*..
gi 300797828 752 eyVLDFYDKYYPLESTECKHAFFLRLR 778
Cdd:COG1246  108 --EIDKEDLPYAKVWQRDSVVMEKDLE 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
681-749 2.04e-09

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.91  E-value: 2.04e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300797828 681 IVAFGFMVPDVkYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCM---GKDVTLHVSASNPAML-LYQKFGFK 749
Cdd:COG3393    2 LVAMAGVRAES-PGVAEISGVYTHPEYRGRGLASALVAALAREALargARTPFLYVDADNPAARrLYERLGFR 73
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 666-761 2.25e-09

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.22  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 666 LQYPDFSVVVLYKKVIVAFG--FMVPDvkyNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASNP-A 739
Cdd:COG0454   30 SLAGAEFIAVDDKGEPIGFAglRRLDD---KVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTaleLDTLDGNPaA 106

                         90       100
                 ....*....|....*....|...
gi 300797828 740 MLLYQKFGFK-TEEYVLDFYDKY 761
Cdd:COG0454  107 IRFYERLGFKeIERYVAYVGGEF 129
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 673-749 2.31e-09

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 54.77  E-value: 2.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300797828  673 VVVLYKKVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTL-HVSASNPAMLLYQKFGFK 749
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLlELETTNRAAAFYEKLGFE 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
641-759 1.26e-08

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 54.32  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 641 RPNHIPTINSMCQEFFWPG--IDLSECLQ---YPDFSVVVLYKKVIVAFGFMVP---DVKYNEAYISFLLVHPEWRRAGI 712
Cdd:COG3153    5 TPEDAEAIAALLRAAFGPGreAELVDRLRedpAAGLSLVAEDDGEIVGHVALSPvdiDGEGPALLLGPLAVDPEYRGQGI 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 300797828 713 ATFMIYHLIQTCMGKDVT-LHVSASNPAMLLYQKFGFK-TEEYVLDFYD 759
Cdd:COG3153   85 GRALMRAALEAARERGARaVVLLGDPSLLPFYERFGFRpAGELGLTLGP 133
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 671-750 3.18e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 46.88  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828  671 FSVVVLYKKVIVAFGFMvpdvkYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTLH---VSASNPAMLLYQKFG 747
Cdd:pfam13673  32 FFFVAFEGGQIVGVIAL-----RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSeltVNASPYAVPFYEKLG 106


                  ...
gi 300797828  748 FKT 750
Cdd:pfam13673 107 FRA 109
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
673-760 6.33e-06

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 46.91  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 673 VVVLYKKVIVAFGFMVP---DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASNPAML-LYQK 745
Cdd:COG1247   55 LVAEEDGEVVGFASLGPfrpRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRrlvAVVLADNEASIaLYEK 134

                         90
                 ....*....|....*
gi 300797828 746 FGFKTEEYVLDFYDK 760
Cdd:COG1247  135 LGFEEVGTLPEVGFK 149
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 672-724 1.36e-05

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 43.42  E-value: 1.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300797828 672 SVVVLYKKVIVAFGFMVP-DVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTC 724
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
694-756 4.69e-05

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.63  E-value: 4.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300797828 694 NEAYISFLLVHPEWRRAGIATFMIYHLIQTCM---GKDVTLHvsASNPAMLLYQKFGFKT--EEYVLD 756
Cdd:COG2153   57 GEAKIGRVAVLPEYRGQGLGRALMEAAIEEARergARRIVLS--AQAHAVGFYEKLGFVPvgEEFLEA 122
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 684-779 6.61e-05

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 44.22  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 684 FGFMVPDVKYNEAYISFLLvHPEWRRAGIATFMIYHLIQTC---MG-KDVTLHVSASNPAML-LYQKFGFKTEEYVldfy 758
Cdd:COG1670   77 VGLYDIDRANRSAEIGYWL-APAYWGKGYATEALRALLDYAfeeLGlHRVEAEVDPDNTASIrVLEKLGFRLEGTL---- 151

                         90       100
                 ....*....|....*....|.
gi 300797828 759 DKYYPLESTECKHAFFLRLRR 779
Cdd:COG1670  152 RDALVIDGRYRDHVLYSLLRE 172
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 688-750 3.86e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.94  E-value: 3.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300797828  688 VPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTLHV-SASNPAMllYQKFGFKT 750
Cdd:pfam13527  63 VPGKTLPAAGITGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFlYPSSYPI--YRRFGYEI 124
PRK09831 PRK09831
GNAT family N-acetyltransferase;
601-763 4.09e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 38.40  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 601 RDYetKPPKLQLLSQI--RSHLHKSDPHWTPEPDAPldycyvrpnhiptinsmcqeffWPGIDLSECLQYPDFSVVvlyk 678
Cdd:PRK09831   4 RNY--QPGDFQQLCAIfiRAVTMTASQHYSPQQIAA----------------------WAQIDESRWKEKLAKSQV---- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 679 KVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTcmgkDVTLHVSASNPAMLLYQKFGFKT-------- 750
Cdd:PRK09831  56 RVAVINAQPVGFITCIEHYIDMLFVDPEYTRRGVASALLKPLIKS----ESELTVDASITAKPFFERYGFQTvkqqrvec 131

                        170
                 ....*....|....
gi 300797828 751 -EEYVLDFYDKYYP 763
Cdd:PRK09831 132 rGEWFINFYMRYKP 145
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 685-763 6.81e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797828 685 GFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVT---LHVSASN-PAMLLYQKFGFKTeeyvLDFYDK 760
Cdd:PRK09491  53 AFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVAtlwLEVRASNaAAIALYESLGFNE----VTIRRN 128


                 ...
gi 300797828 761 YYP 763
Cdd:PRK09491 129 YYP 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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